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Immunology. 1994 Jan;81(1):137-41.

Glycosylation of IgA is required for optimal activation of the alternative complement pathway by immune complexes.

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1
Molecular Immunopathology Unit, MRC Centre, Cambridge, U.K.

Abstract

To investigate the effect of carbohydrate on activation of the alternative pathway of complement by IgA immune complexes, aglycosylated monoclonal IgA was made biosynthetically in the presence of tunicamycin. When immune complexes were incubated with normal human serum (NHS), the aglycosylated IgA immune complexes caused less depletion of the alternative pathway activity of the serum. They also bound less C3 and produced less terminal complement complexes. The binding of C3 to both immune complexes was mainly through hydroxylamine sensitive ester bonds. C3 did not bind to free IgA.

PMID:
8132210
PMCID:
PMC1422296
[Indexed for MEDLINE]
Free PMC Article
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